News

Split-Second Reactions

Burrowed deep under the foothills near Palo Alto, Calif., scientists scurried through an underground laboratory, making final preparations for a series of explosions. THEIR PLAN: blow up tiny crystals of proteins that could reveal one of nature's best-kept secrets—how plant photosynthesis turns light into chemical energy. The potential payoff: a step toward unlimited clean power.

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Moving in the Right Direction: Protein Vibrational Steering Function

Nearly all protein functions require structural change, such as enzymes clamping onto substrates, and ion channels opening and closing. These motions are a target for possible new therapies; however, the control mechanisms are under debate. Calculations have indicated protein vibrations enable structural change. However, previous measurements found these vibrations only weakly depend on the functional state.

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Diffraction data of core-shell nanoparticles from an X-ray free electron laser

X-ray free-electron lasers provide novel opportunities to conduct single particle analysis on nanoscale particles. Coherent diffractive imaging experiments were performed at the Linac Coherent Light Source (LCLS), SLAC National Laboratory, exposing single inorganic core-shell nanoparticles to femtosecond hard-X-ray pulses.

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BioXFEL CoPI Appointed to DOE Advisory Committee

Abbas Ourmazd, a UWM distinguished professor of physics, has been appointed to serve on the Basic Energy Sciences Advisory Committee (BESAC) of the U.S. Department of Energy (DOE). The 25-member committee has a substantial impact on national scientific programs, supporting more than 2,500 principal investigators in physics, chemistry, geology and biosciences at 165 institutions in 49 states and 14 DOE laboratories.

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Bacterial expression, correct membrane targeting and functional folding of the HIV-1 membrane protein Vpu using a periplasmic signal peptide

Structural analysis of membrane proteins has traditionally been bottlenecked by the lack of sufficiently large amounts of pure, properly folded and functional membrane proteins. The issue is particularly important considering the fact that membrane proteins constitute a significant proportion of clinical drug targets.

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BioXFEL collaborator Henry Chapman receives 2017 Roentgen Medal

DESY scientist Henry Chapman has been awarded the Roentgen Medal by the city of Remscheid. The town in which Wilhelm Conrad Roentgen was born has been presenting this award annually since 1951 to individuals who have made outstanding contributions towards improving and advancing the use of the radiation discovered by Roentgen. Henry Chapman, a Leading Scientist at DESY and professor at the University of Hamburg, has been awarded the Medal in recognition of his pioneering work on the application of X-ray lasers for determining the structure of biological macromolecules. 

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